A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division

Huijia Yin, Yang Liu, Ying Zhao, Pengyue Chen and Zengyi Chang ()
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Huijia Yin: Peking University
Yang Liu: Peking University
Ying Zhao: Peking University
Pengyue Chen: Peking University
Zengyi Chang: Peking University

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Bacterial cell division hinges on the Z-ring, an architecture built from the dynamical assembly and disassembly of FtsZ proteins. This delicate balance ensures not only apparent stability, but also continuous remodeling, both of which are required for Z-ring functioning. However, the molecular nature of such subcellular structures remains elusive. Here, by identifying all amino acid residues participating in FtsZ self-assembly in Escherichia coli, we show that the extreme N-terminal intrinsically disordered region (N-IDR) of FtsZ acts as a cis disassembly element that contacts and disrupts the longitudinal interface, tipping the balance more toward polymer disassembly. This previously unappreciated structural characteristic is indispensable for promoting Z-ring architecture condensation at midcell (rather than elsewhere) upon modulation by certain trans-acting factors (such as the E. coli MinC protein).

Date: 2025
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DOI: 10.1038/s41467-025-60517-7

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